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{"title"=>"Chemical magnetoreception: Bird cryptochrome 1a is excited by blue light and forms long-lived radical-pairs", "type"=>"journal", "authors"=>[{"first_name"=>"Miriam", "last_name"=>"Liedvogel", "scopus_author_id"=>"6508097950"}, {"first_name"=>"Kiminori", "last_name"=>"Maeda", "scopus_author_id"=>"7404376029"}, {"first_name"=>"Kevin", "last_name"=>"Henbest", "scopus_author_id"=>"6506678793"}, {"first_name"=>"Erik", "last_name"=>"Schleicher", "scopus_author_id"=>"7005303336"}, {"first_name"=>"Thomas", "last_name"=>"Simon", "scopus_author_id"=>"57197473265"}, {"first_name"=>"Christiane R.", "last_name"=>"Timmel", "scopus_author_id"=>"6602348797"}, {"first_name"=>"P. J.", "last_name"=>"Hore", "scopus_author_id"=>"7006943401"}, {"first_name"=>"Henrik", "last_name"=>"Mouritsen", "scopus_author_id"=>"6602169142"}], "year"=>2007, "source"=>"PLoS ONE", "identifiers"=>{"issn"=>"19326203", "scopus"=>"2-s2.0-42549166971", "sgr"=>"42549166971", "pui"=>"351586848", "isbn"=>"1932-6203 (Electronic)", "pmid"=>"17971869", "doi"=>"10.1371/journal.pone.0001106"}, "id"=>"af9a4b60-cf2d-3a7a-8c50-39a013c297fb", "abstract"=>"Cryptochromes (Cry) have been suggested to form the basis of light-dependent magnetic compass orientation in birds. However, to function as magnetic compass sensors, the cryptochromes of migratory birds must possess a number of key biophysical characteristics. Most importantly, absorption of blue light must produce radical pairs with lifetimes longer than about a microsecond. Cryptochrome 1a (gwCry1a) and the photolyase-homology-region of Cry1 (gwCry1-PHR) from the migratory garden warbler were recombinantly expressed and purified from a baculovirus/Sf9 cell expression system. Transient absorption measurements show that these flavoproteins are indeed excited by light in the blue spectral range leading to the formation of radicals with millisecond lifetimes. These biophysical characteristics suggest that gwCry1a is ideally suited as a primary light-mediated, radical-pair-based magnetic compass receptor.", "link"=>"http://www.mendeley.com/research/chemical-magnetoreception-bird-cryptochrome-1a-excited-blue-light-forms-longlived-radicalpairs", "reader_count"=>152, "reader_count_by_academic_status"=>{"Unspecified"=>4, "Professor > Associate Professor"=>8, "Librarian"=>1, "Researcher"=>39, "Student > Doctoral Student"=>8, "Student > Ph. D. Student"=>36, "Student > Postgraduate"=>4, "Student > Master"=>17, "Other"=>7, "Student > Bachelor"=>20, "Lecturer"=>4, "Professor"=>4}, "reader_count_by_user_role"=>{"Unspecified"=>4, "Professor > Associate Professor"=>8, "Librarian"=>1, "Researcher"=>39, "Student > Doctoral Student"=>8, "Student > Ph. D. Student"=>36, "Student > Postgraduate"=>4, "Student > Master"=>17, "Other"=>7, "Student > Bachelor"=>20, "Lecturer"=>4, "Professor"=>4}, "reader_count_by_subject_area"=>{"Unspecified"=>6, "Agricultural and Biological Sciences"=>76, "Arts and Humanities"=>1, "Chemistry"=>25, "Earth and Planetary Sciences"=>1, "Engineering"=>5, "Environmental Science"=>3, "Biochemistry, Genetics and Molecular Biology"=>10, "Materials Science"=>1, "Medicine and Dentistry"=>6, "Neuroscience"=>5, "Pharmacology, Toxicology and Pharmaceutical Science"=>1, "Physics and Astronomy"=>12}, "reader_count_by_subdiscipline"=>{"Materials Science"=>{"Materials Science"=>1}, "Medicine and Dentistry"=>{"Medicine and Dentistry"=>6}, "Physics and Astronomy"=>{"Physics and Astronomy"=>12}, "Unspecified"=>{"Unspecified"=>6}, "Environmental Science"=>{"Environmental Science"=>3}, "Pharmacology, Toxicology and Pharmaceutical Science"=>{"Pharmacology, Toxicology and Pharmaceutical Science"=>1}, "Arts and Humanities"=>{"Arts and Humanities"=>1}, "Engineering"=>{"Engineering"=>5}, "Chemistry"=>{"Chemistry"=>25}, "Neuroscience"=>{"Neuroscience"=>5}, "Earth and Planetary Sciences"=>{"Earth and Planetary Sciences"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>76}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>10}}, "reader_count_by_country"=>{"Sweden"=>1, "United States"=>5, "Egypt"=>1, "Chile"=>1, "Germany"=>4, "Spain"=>1, "India"=>1}, "group_count"=>4}

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• {"id"=>"1028414172277755906", "text"=>"RT @foodtechhacker: https://t.co/WHVkOVnjm8\n\nhttps://t.co/Oo7iLBj2PQ\n\nhttps://t.co/o0XAWEVfIq\n\nhttps://t.co/oq3Le7iCvz\n\n@ajwodecki @DrJackK…", "created_at"=>"2018-08-11T22:53:40Z", "user"=>"richardursomd", "user_name"=>"Dr. Urso", "user_profile_image"=>"http://pbs.twimg.com/profile_images/823256918097620992/nD_HObEo_normal.jpg"}
• {"id"=>"1036042493094232064", "text"=>"#PLOSONE: Chemical Magnetoreception: Bird Cryptochrome 1a Is Excited by Blue Light and Forms Long-Lived Radic ... https://t.co/dHWcvnzQZr", "created_at"=>"2018-09-02T00:05:53Z", "user"=>"jbruhaha94", "user_name"=>"J Bruha", "user_profile_image"=>"http://pbs.twimg.com/profile_images/2553842007/f8olmpcla546l3crt1hm_normal.jpeg"}
• {"id"=>"984528067782639617", "text"=>"Birds can see North/South within 5? precision: https://t.co/Can6zaBY3S https://t.co/6wE0hO4fGB", "created_at"=>"2018-04-12T20:25:57Z", "user"=>"danfolkes", "user_name"=>"danfolkes", "user_profile_image"=>"http://pbs.twimg.com/profile_images/700011894443216896/FlLlqJ6m_normal.jpg"}
• {"id"=>"994292864547880960", "text"=>"https://t.co/WHVkOVnjm8\n\nhttps://t.co/Oo7iLBj2PQ\n\nhttps://t.co/o0XAWEVfIq\n\nhttps://t.co/oq3Le7iCvz\n\n@ajwodecki @DrJackKruse @erreyedoc", "created_at"=>"2018-05-09T19:07:46Z", "user"=>"foodtechhacker", "user_name"=>"Galen Z", "user_profile_image"=>"http://pbs.twimg.com/profile_images/939699524892688384/x9p_EU-w_normal.jpg"}
• {"id"=>"994588047608922113", "text"=>"RT @foodtechhacker: https://t.co/WHVkOVnjm8\n\nhttps://t.co/Oo7iLBj2PQ\n\nhttps://t.co/o0XAWEVfIq\n\nhttps://t.co/oq3Le7iCvz\n\n@ajwodecki @DrJackK…", "created_at"=>"2018-05-10T14:40:43Z", "user"=>"ajwodecki", "user_name"=>"RealFoodOptometrist", "user_profile_image"=>"http://pbs.twimg.com/profile_images/559518707307642880/AvN5wA62_normal.jpeg"}
• {"id"=>"994590440287621120", "text"=>"@foodtechhacker @DrJackKruse @erreyedoc ?? https://t.co/SNAWsTmJ5L", "created_at"=>"2018-05-10T14:50:14Z", "user"=>"ajwodecki", "user_name"=>"RealFoodOptometrist", "user_profile_image"=>"http://pbs.twimg.com/profile_images/559518707307642880/AvN5wA62_normal.jpeg"}

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Figshare

• {"files"=>["https://ndownloader.figshare.com/files/943528"], "description"=>"<p>A Transient absorption spectra for <i>gw</i>Cry1a as a function of wavelength (monitoring beam) proves that radical pairs are produced in cryptochromes of a migratory bird. The five graphs reflect the optical properties of the sample at different times, <i>t</i>_delay, after the laser flash. The amplitude of the signals depends on the protein concentration. The spectra were obtained by averaging two time profiles (cf. Fig. 1B) centred at <i>t</i>_delay using a time window of 500 µs. The variation of the absorption signal is about 5%, which is estimated from the data at 0.5 ms from 500 to 600 nm. For a detailed analysis of the spectra, see main text. B Transient absorption time profiles for <i>gw</i>Cry1a. A laser flash (indicated by the arrow) is given at time = 0. The transient signal is obtained by averaging 7 time-profiles for the 490–550 nm wavelength region (corresponding to the optical features framed in blue in Fig. 1A) in 10 nm steps (blue curve, left scale) and 9 time-profiles for the 550–630 nm region (corresponding to the optical features framed in red in Fig. 1A) in 10 nm steps (red, graph, right scale), respectively. Solid lines show the fitted single or double exponential decays. The laser flash leads to radical formation as reflected by positive changes in the absorption signal. Significant radical concentrations are detectable up to ∼25 ms. For further discussion, see main text.</p>", "links"=>[], "tags"=>["absorption", "spectra"], "article_id"=>613926, "categories"=>["Biochemistry", "Biophysics", "Infectious Diseases"], "users"=>["Miriam Liedvogel", "Kiminori Maeda", "Kevin Henbest", "Erik Schleicher", "Thomas Simon", "Christiane R. Timmel", "P. J. Hore", "Henrik Mouritsen"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0001106.g001", "stats"=>{"downloads"=>1, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Transient_absorption_spectra_for_gw_Cry1a_/613926", "title"=>"Transient absorption spectra for <i>gw</i>Cry1a.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2007-10-31 01:05:26"}
• {"files"=>["https://ndownloader.figshare.com/files/943708"], "description"=>"<p>A Sequence alignment of Cry1a of two migratory songbird species <i>Sylvia borin</i> (Garden warbler; GenBank accession no. AJ632120), <i>Erithacus rubecula</i> (European robin; AY585716), Cry1 of <i>Arabidopsis thaliana</i> (mouse-ear cress; Q43125) and DNA photolyase of <i>Escherichia coli</i> (P00914). The alignment shows that all three members of the Trp-triad electron transfer chain known to be involved in intraprotein electron transfer during signalling through photoreduction in both <i>E. coli</i> photolyse and <i>At</i>Cry1 are clearly present in the Cry1a sequences of both migratory bird species (Trp-397, Trp-374, Trp-321). B Reaction scheme for <i>gw</i>Cry1a (adapted from a very similar scheme for <i>At</i>Cry1 proposed by Giovani <i>et al. </i><a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0001106#pone.0001106-Lin2\" target=\"_blank\">[36]</a>). Processes directly observed here are represented by solid arrows. Other steps are indicated by dashed arrows <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0001106#pone.0001106-Lin2\" target=\"_blank\">[36]</a>. The excited state of the FAD is assumed here to be a <i>singlet</i>; an almost identical scheme would result if, instead, <i>triplet</i> FAD were assumed to be the photoactive excited state. Singlet-triplet interconversion in the [FADH^• Trp^•] radical pair is indicated by the curved block arrows. D and A are respectively an external electron donor and acceptor.</p>", "links"=>[], "tags"=>["alignment", "members"], "article_id"=>614108, "categories"=>["Biochemistry", "Biophysics", "Infectious Diseases"], "users"=>["Miriam Liedvogel", "Kiminori Maeda", "Kevin Henbest", "Erik Schleicher", "Thomas Simon", "Christiane R. Timmel", "P. J. Hore", "Henrik Mouritsen"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0001106.g004", "stats"=>{"downloads"=>1, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Sequence_alignment_between_different_members_and_species_within_the_cryptochrome_photolyase_protein_family_/614108", "title"=>"Sequence alignment between different members and species within the cryptochrome/photolyase protein family.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2007-10-31 01:08:28"}
• {"files"=>["https://ndownloader.figshare.com/files/943583"], "description"=>"<p>A Coomassie stained SDS gel, and B Western-blot (with α-Cry1 antiserum from immunised goat), both showing identical fractions of the IMAC purification process. <i>gw</i>Cry1a (628 aa) is recognisable as a distinct band at ∼62 kDa in both the coomassie stained SDS gel and on the Western-blot (indicated by the arrowhead to the right). <i>1: gw</i>Cry1a lysate (protein extract from insect cell pellet, 1∶10 dilution); <i>2: gw</i>Cry1a cleared lysate (centrifuged and filtered lysate, 1∶10 dilution); <i>3: gw</i>Cry1a flow through (after sample loading on column, 1∶10 dilution); <i>4: gw</i>Cry1a elution step1 (e1) [75% imidazole]; <i>5: gw</i>Cry1a elution step2 (e2) [100% imidazole] protein quantity for e2 is 5 µg; <i>6:</i> negative control (recombinantly expressed human La/SSB autoantigen; ∼48 kDa) confirms the specificity of the antibody.</p>", "links"=>[], "tags"=>["recombinantly", "warbler", "cryptochrome"], "article_id"=>613977, "categories"=>["Biochemistry", "Biophysics", "Infectious Diseases"], "users"=>["Miriam Liedvogel", "Kiminori Maeda", "Kevin Henbest", "Erik Schleicher", "Thomas Simon", "Christiane R. Timmel", "P. J. Hore", "Henrik Mouritsen"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0001106.g002", "stats"=>{"downloads"=>1, "page_views"=>14, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_SDS_PAGE_of_recombinantly_expressed_garden_warbler_cryptochrome_shown_for_gw_Cry1a_protein_/613977", "title"=>"SDS-PAGE of recombinantly expressed garden warbler cryptochrome (shown for <i>gw</i>Cry1a protein).", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2007-10-31 01:06:17"}
• {"files"=>["https://ndownloader.figshare.com/files/464316", "https://ndownloader.figshare.com/files/464371", "https://ndownloader.figshare.com/files/464410"], "description"=>"<div><p>Cryptochromes (Cry) have been suggested to form the basis of light-dependent magnetic compass orientation in birds. However, to function as magnetic compass sensors, the cryptochromes of migratory birds must possess a number of key biophysical characteristics. Most importantly, absorption of blue light must produce radical pairs with lifetimes longer than about a microsecond. Cryptochrome 1a (<em>gw</em>Cry1a) and the photolyase-homology-region of Cry1 (<em>gw</em>Cry1-PHR) from the migratory garden warbler were recombinantly expressed and purified from a baculovirus/<em>Sf9</em> cell expression system. Transient absorption measurements show that these flavoproteins are indeed excited by light in the blue spectral range leading to the formation of radicals with millisecond lifetimes. These biophysical characteristics suggest that <em>gw</em>Cry1a is ideally suited as a primary light-mediated, radical-pair-based magnetic compass receptor.</p></div>", "links"=>[], "tags"=>["cryptochrome", "1a", "forms", "long-lived", "radical-pairs"], "article_id"=>151514, "categories"=>["Biochemistry", "Biophysics", "Cancer"], "users"=>["Miriam Liedvogel", "Kiminori Maeda", "Kevin Henbest", "Erik Schleicher", "Thomas Simon", "Christiane R. Timmel", "P. J. Hore", "Henrik Mouritsen"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0001106.s001", "https://dx.doi.org/10.1371/journal.pone.0001106.s002", "https://dx.doi.org/10.1371/journal.pone.0001106.s003"], "stats"=>{"downloads"=>20, "page_views"=>9, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Chemical_Magnetoreception_Bird_Cryptochrome_1a_Is_Excited_by_Blue_Light_and_Forms_Long_Lived_Radical_Pairs/151514", "title"=>"Chemical Magnetoreception: Bird Cryptochrome 1a Is Excited by Blue Light and Forms Long-Lived Radical-Pairs", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2007-10-31 00:25:14"}
• {"files"=>["https://ndownloader.figshare.com/files/943646"], "description"=>"<p>A <i>gw</i>Cry1-PHR, illumination time: 0 s (black), 40 s (yellow), 80 s (orange), 130 s (light blue), 190 s (blue) and 340 s (green), respectively. B <i>gw</i>Cry1a, illumination time: 0 s (black), 90 s (yellow), 150 s (orange), 240 s (light blue), 360 s (blue) and 540 s (green), respectively. Both samples were illuminated under anaerobic conditions as indicated in the Methods section. Reoxidation was achieved by bubbling air into the optical cuvette (red dashed lines).</p>", "links"=>[], "tags"=>["spectroscopy", "cryptochrome", "holoprotein", "migratory"], "article_id"=>614041, "categories"=>["Biochemistry", "Biophysics", "Infectious Diseases"], "users"=>["Miriam Liedvogel", "Kiminori Maeda", "Kevin Henbest", "Erik Schleicher", "Thomas Simon", "Christiane R. Timmel", "P. J. Hore", "Henrik Mouritsen"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0001106.g003", "stats"=>{"downloads"=>2, "page_views"=>9, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Optical_spectroscopy_of_cryptochrome_holoprotein_from_migratory_garden_warblers_/614041", "title"=>"Optical spectroscopy of cryptochrome holoprotein from migratory garden warblers.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2007-10-31 01:07:21"}

PMC Usage Stats | Further Information

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Relative Metric

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F1000Prime